Voltage gated potassium channels are a tetramer of proteins that have six transmembrane domains with a p-loop that participates in the formation of the selectivity pore. Voltage-gated sodium channels... a) Share the same building principles, but the primary protein contains all 24 transmembrane domains b) are tetramers like potassium channels c) share no commonality with potassium channels
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Consider a voltage gated K+ channel. Select ALL the answers that are TRUE regarding this transmembrane protein. a It's transmembrane domain has both hydrophobic and hydrophilic R-groups. b It's transmembrane domain includes alpha-helical secondary structure. c It's transmembrane domain forms a channel that is always open. d It contains specific amino acids that forms a region that selelcts for K+ ions.
Shaiju T.
1) Hypothesize why potassium channels have evolved to be tetrameric? 2) Explain why the amino acids that "carry" the positive gating charges in the potassium channel voltage sensors are arginines and not lysines? 3) Explain how potassium channels can be thought of as enzymes. Your explanation should apply principles of enzyme catalysis to the structure and function of the potassium channel pore domain.
Suman K.
Write a detailed description of the biogenesis of a typical voltage-gated potassium channel found in the plasma membrane of animal cells. The description should begin with the gene for the channel protein and end with the channel in its final location in the plasma membrane. Your description should be between 300 and 500 words long. It should be written for upper division biology students (i.e. your peers). It should be entirely your own original writing. Do not copy or paraphrase your classmates or any other resource. Here's what you need to know about the typical voltage-gated potassium (KV) channel to write your description: KV channels are 6-pass transmembrane proteins found in the plasma membrane. The KV gene contains 14 introns. The 6 transmembrane domains are alpha-helices that include mainly hydrophobic amino acids. Both the N-terminus and C-terminus of the protein face the cytosol. Portions of the protein on the extracellular face are glycosylated. Initial glycosylation of the KV channel occurs in the ER. Further glycosylation and sialylation (addition of a sialic acid group) occur in the Golgi. The extracellular regions of the protein form several disulfide bonds.
Sri K.
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